ID   C3PFK2_CORA7            Unreviewed;      1120 AA.
AC   C3PFK2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-OCT-2025, entry version 84.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:ACP32606.1};
DE            EC=1.2.4.2 {ECO:0000313|EMBL:ACP32606.1};
GN   Name=sucA {ECO:0000313|EMBL:ACP32606.1};
GN   OrderedLocusNames=cauri_1009 {ECO:0000313|EMBL:ACP32606.1};
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS   CN-1) (Corynebacterium nigricans).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP32606.1, ECO:0000313|Proteomes:UP000002077};
RN   [1] {ECO:0000313|EMBL:ACP32606.1, ECO:0000313|Proteomes:UP000002077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC   {ECO:0000313|Proteomes:UP000002077};
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA   Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA   Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT   aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT   vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00052761};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051911};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC       CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004813}.
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DR   EMBL; CP001601; ACP32606.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3PFK2; -.
DR   STRING; 548476.cauri_1009; -.
DR   KEGG; car:cauri_1009; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000002077; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACP32606.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          767..963
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1120 AA;  123942 MW;  0822E43DC174B79B CRC64;
     MFKAIAKNMD ESLEIPTATT VRDIPVKLMW ENRAMINDHL KRTRGGKISF THILGYALVK
     AVQIHPDMNV RYELQDGKPT VVQPEHVNLG LAIDLPQKDG SRALVVAAIK EAENKTFSEF
     IDAYQDIVDR SRKNKLTMDD FSGVTINLTN PGGIGTRHSI ARLTKGSGSI IGVGSMDYPA
     EFAGTSADRL ADLGVGRLVT LTSTYDHRVI QGAESGEFLR TVGQLILDDA FWDELFESMG
     VPYQPFRWAA DVPNTGVDKN TRVMQYIEAY RSRGHLLADI NPLGWKQPGL PWPDHRDLDL
     ATHGLTIWDL DRTFNVGGFG GKETMTLREV VTRLRSAYTL KVGSEYAHIL DRDERGWLQE
     QIEAGMPKPT NSEQKYILQK VNAAEAFENF LQTKYVGQKR FSLEGAESLI ALLDSIVDTA
     AGQDLDEVVI GMPHRGRLNV LFNIVGKPLA DIFGEFDGNY KGGQMGGSGD VKYHLGAEGE
     HLQMFGDGEI KVTLAANPSH LEAVDPVMEG IARAKQDILD KGAEGHTVVP IMLHGDASFT
     GLGVVQETIN LSQLRGYTTG GTVHVVVNNQ VGFTTTPDSG RSTHYATDLA KGFDCPVFHV
     NGDNPEAVVW VGKLATEYRR RFGKDVFIDL VCYRLRGHNE ADDPSMTQPQ LYDIIDDHKS
     VRERYTEELI GRGDLSDEEA EAAARDFHDQ MESVFADHKK AEEAGPKEQT GITSSQELTR
     GLDTSITAEE LAEIGDAYGT PPEGFEYHKR VAKVAKDRQK SSREGGIDWG WGELIAFGSL
     ANSGKVVRLA GEDSRRGTFT QRHAVAFDPR TGEEHNPVAH LAKSKGNGGK FMVYNSALTE
     FAGMGFEYGY TVGNPDAVVA WEAQFGDFAN GAQTIIDEYV SSGEAKWGQL SSLILLLPHG
     YEGQGPDHSS ARIERFLQLC AEGSMTVAQP STPANHFHLL RRQALGEMKR PLVVFTPKSM
     LRNKAATSSV EDFTEVKKFQ SVINDPNFVD IKGKKVGDTD KVKTIMLVSG KLYWELAKKK
     EADGRDDIAI VRVEMLHPIP FNRLREAFEA YPNATQIRFV QDEPANQGPW PFYNEHLRDL
     IPDMPEMVRV SRRSQSSTAT GNAKVHQIEQ KNLLEEAFDV
//